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Diverse Protein Architectures and α- N -Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters.

Aman S ImaniAileen R LeeNisha VishwanathanFloris de WaalMichael F Freeman
Published in: ACS chemical biology (2022)
Borosins are ribosomally synthesized and post-translationally modified peptides (RiPPs) with α- N -methylations installed on the peptide backbone that impart unique properties like proteolytic stability to these natural products. The borosin RiPP family was initially reported only in fungi until our recent discovery and characterization of a Type IV split borosin system in the metal-respiring bacterium Shewanella oneidensis . Here, we used hidden Markov models and sequence similarity networks to identify over 1600 putative pathways that show split borosin biosynthetic gene clusters are widespread in bacteria. Noteworthy differences in precursor and α- N -methyltransferase open reading frame sizes, architectures, and core peptide properties allow further subdivision of the borosin family into six additional discrete structural types, of which five have been validated in this study.
Keyphrases
  • genome wide
  • copy number
  • amino acid
  • genome wide identification
  • dna methylation
  • small molecule
  • minimally invasive
  • working memory
  • transcription factor
  • binding protein
  • genome wide analysis